Institutional Publications

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Author: search.filters.author.Puranik, SwatiSubject: search.filters.subject.WD40 protein

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    Structure and regulatory networks of WD40 protein in plants
    (Springer, 2012) Mishra, Awdhesh Kumar; Puranik, Swati; Prasad, Manoj
    Plants have been gifted with intricate regulatory networks to carry on with their sessile life form. Often such networks involve delicate association between various proteins. The WD40 proteins, which are present abundantly in several eukaryotes, act as scaffolding molecules assisting proper activity of other proteins. They comprise several stretches of 44–60 amino acid residues and often terminate with a WD dipeptide. They function in several cellular, metabolic and molecular pathways, biologically playing important roles in plant development and also during stress signaling. Moreover, some WD40 (named DWD) proteins also function as substrate receptors in Cullin4 RING dependent E3 ubiquitin ligase mediated proteosomal degradation and DNA damage repair mechanism. In this review, we have discussed the various aspects of these proteins that affect their highly diversified functions in plants.
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    The DNA-binding activity of an AP2 protein is involved in transcriptional regulation of a stress-responsive gene, SiWD40, in foxtail millet
    (Elsevier, 2012) Mishra, Awdhesh Kumar; Puranik, Swati; Bahadur, Ranjit Prasad; Prasad, Manoj
    A differentially expressed transcript, encoding a putative WD protein (Setaria italica WD40; SiWD40), was identified in foxtail millet. Tertiary structure modeling revealed that its C-terminus possesses eight blade β-propeller architecture. Its N-terminal has three α-helices and two 310-helices and was highly induced by different abiotic stresses. The SiWD40:GFP fusion protein was nuclear localized. Promoter analysis showed the presence of many cis-acting elements, including two dehydration responsive elements (DRE). A stress-responsive SiAP2 domain containing protein could specifically bind to these elements in the SiWD40 promoter. Thus, for the first time, we report that DREs probably regulate expression of SiWD40 during envi- ronmental stress. Molecular docking analysis revealed that the circumference of the β‐propeller structure was involved in an interaction with a SiCullin4 protein, supporting the adaptability of SiWD40 to act as a scaf- fold. Our study thus provides a vital clue for near future research on the stress-regulation of WD proteins.